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Tissue-specific phosphorylation of complement receptors CR1 and CR2
CR1 of neutrophils and monocytes may exist in a resting state, in which it only binds ligand-coated particles, or an activated state, in which it mediates phagocytosis. Because the activated state of CR1 can be induced by the stimulation of protein kinase C with PMA, CR1 was assessed for phosphoryla...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1986
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188014/ https://www.ncbi.nlm.nih.gov/pubmed/3484510 |
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collection | PubMed |
description | CR1 of neutrophils and monocytes may exist in a resting state, in which it only binds ligand-coated particles, or an activated state, in which it mediates phagocytosis. Because the activated state of CR1 can be induced by the stimulation of protein kinase C with PMA, CR1 was assessed for phosphorylation. Purified human neutrophils, monocytes, eosinophils, tonsilar lymphocytes, SB cells, and erythrocytes were labeled with 32PO4 and incubated with buffer or 100 ng/ml PMA. Membrane proteins were immunoprecipitated and analyzed by SDS-PAGE and autoradiography. CR1, unlike HLA class I heavy chain, was not constitutively phosphorylated by any cell type. PMA induced phosphorylation of CR1 in three phagocytic cell types, but did not induce the phosphorylation of CR3 or FcR. FMLP also induced the phosphorylation of CR1 in neutrophils. In contrast, PMA did not induce phosphorylation of CR1 in tonsilar B lymphocytes, SB cells, or erythrocytes, indicating restriction of this reaction to phagocytic cell types. This may be due to differences in the structure or presentation of the cytoplasmic domain of CR1 in phagocytic vs. nonphagocytic cells. Phosphorylation of CR2, however, did occur in PMA- treated B lymphocytes and SB cells, suggesting that this receptor, rather than CR1, may be involved in regulation of B lymphocyte function. |
format | Text |
id | pubmed-2188014 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1986 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21880142008-04-17 Tissue-specific phosphorylation of complement receptors CR1 and CR2 J Exp Med Articles CR1 of neutrophils and monocytes may exist in a resting state, in which it only binds ligand-coated particles, or an activated state, in which it mediates phagocytosis. Because the activated state of CR1 can be induced by the stimulation of protein kinase C with PMA, CR1 was assessed for phosphorylation. Purified human neutrophils, monocytes, eosinophils, tonsilar lymphocytes, SB cells, and erythrocytes were labeled with 32PO4 and incubated with buffer or 100 ng/ml PMA. Membrane proteins were immunoprecipitated and analyzed by SDS-PAGE and autoradiography. CR1, unlike HLA class I heavy chain, was not constitutively phosphorylated by any cell type. PMA induced phosphorylation of CR1 in three phagocytic cell types, but did not induce the phosphorylation of CR3 or FcR. FMLP also induced the phosphorylation of CR1 in neutrophils. In contrast, PMA did not induce phosphorylation of CR1 in tonsilar B lymphocytes, SB cells, or erythrocytes, indicating restriction of this reaction to phagocytic cell types. This may be due to differences in the structure or presentation of the cytoplasmic domain of CR1 in phagocytic vs. nonphagocytic cells. Phosphorylation of CR2, however, did occur in PMA- treated B lymphocytes and SB cells, suggesting that this receptor, rather than CR1, may be involved in regulation of B lymphocyte function. The Rockefeller University Press 1986-01-01 /pmc/articles/PMC2188014/ /pubmed/3484510 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Tissue-specific phosphorylation of complement receptors CR1 and CR2 |
title | Tissue-specific phosphorylation of complement receptors CR1 and CR2 |
title_full | Tissue-specific phosphorylation of complement receptors CR1 and CR2 |
title_fullStr | Tissue-specific phosphorylation of complement receptors CR1 and CR2 |
title_full_unstemmed | Tissue-specific phosphorylation of complement receptors CR1 and CR2 |
title_short | Tissue-specific phosphorylation of complement receptors CR1 and CR2 |
title_sort | tissue-specific phosphorylation of complement receptors cr1 and cr2 |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188014/ https://www.ncbi.nlm.nih.gov/pubmed/3484510 |